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Q2IKQ7 (PUR9_ANADE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional purine biosynthesis protein PurH

Including the following 2 domains:

  1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
    EC=2.1.2.3
    Alternative name(s):
    AICAR transformylase
  2. IMP cyclohydrolase
    EC=3.5.4.10
    Alternative name(s):
    ATIC
    IMP synthase
    Inosinicase
Gene names
Name:purH
Ordered Locus Names:Adeh_2468
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length524 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. HAMAP-Rule MF_00139

Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.

Domain

The IMP cyclohydrolase activity resides in the N-terminal region By similarity. HAMAP-Rule MF_00139

Sequence similarities

Belongs to the PurH family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 524524Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018834

Sequences

Sequence LengthMass (Da)Tools
Q2IKQ7 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 81A77AAAD34769E7

FASTA52455,984
        10         20         30         40         50         60 
MTRRALVSVS DKTGLVPFAR RLAALGVELL STGGTQKALA EAGVPVTGVG DYTQAPEILG 

        70         80         90        100        110        120 
GRVKTLHPRV HGGILYRRGL ASDEADVKAR DIPPIDLVVV NLYPFREAVA AGKPFETCVE 

       130        140        150        160        170        180 
EIDIGGPTMV RSAAKNSAHV GVVVDPADYD KVAAELEATR ALSDATRFYL MKKAFAHTAA 

       190        200        210        220        230        240 
YDAAISEYLT ARETPEAAPA HFPATLAAVY TKAYDLRYGE NPHQAGAFYR AAREPEEPSV 

       250        260        270        280        290        300 
AFAQVLQGKE LSYNNLLDLQ AALAGVMEFD ETACVVIKHN TPCGVSTGRT AGEAFARARE 

       310        320        330        340        350        360 
CDPVSAFGGI VALNRPVDEA TASELTSLFL ECVIAPGYDA AARAALAVKK NLRLLEAPRL 

       370        380        390        400        410        420 
GAARATWRRR PEEGRELRSI PGGLLVMDRD LGSVRREDCK VMTKRAPTEQ EWKDLLFAWK 

       430        440        450        460        470        480 
VVKHVKSNAI VFAKDDRTVA IGGGQTSRVE SVKTAVMKAA LDVRGSSVGS DAFFPFADGV 

       490        500        510        520 
EEIIKAGATA IIQPGGSMRD AEVIAAADKA GIAMVATGMR HFRH 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2CP-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000251 Genomic DNA. Translation: ABC82238.1.
RefSeqYP_465675.1. NC_007760.1.

3D structure databases

ProteinModelPortalQ2IKQ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290397.Adeh_2468.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC82238; ABC82238; Adeh_2468.
GeneID3890166.
KEGGade:Adeh_2468.
PATRIC20921103. VBIAnaDeh31384_2529.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMACGVATGP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycADEH290397:GI2Z-2499-MONOMER.
UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Family and domain databases

Gene3D3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPMF_00139. PurH.
InterProIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERPTHR11692. PTHR11692. 1 hit.
PfamPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_ANADE
AccessionPrimary (citable) accession number: Q2IKQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 7, 2006
Last modified: May 14, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways